A sulfilimine bond identified in collagen IV.

Vanacore R, Ham AJ, Voehler M, Sanders CR, Conrads TP, Veenstra TD, Sharpless KB, Dawson PE, Hudson BG
Science. 2009 325 (5945): 1230-4

PMID: 19729652 · PMCID: PMC2876822 · DOI:10.1126/science.1176811

Collagen IV networks are ancient proteins of basement membranes that underlie epithelia in metazoa from sponge to human. The networks provide structural integrity to tissues and serve as ligands for integrin cell-surface receptors. They are assembled by oligomerization of triple-helical protomers and are covalently crosslinked, a key reinforcement that stabilizes networks. We used Fourier-transform ion cyclotron resonance mass spectrometry and nuclear magnetic resonance spectroscopy to show that a sulfilimine bond (-S=N-) crosslinks hydroxylysine-211 and methionine-93 of adjoining protomers, a bond not previously found in biomolecules. This bond, the nitrogen analog of a sulfoxide, appears to have arisen at the divergence of sponge and cnidaria, an adaptation of the extracellular matrix in response to mechanical stress in metazoan evolution.

MeSH Terms (19)

Amino Acid Sequence Animals Cattle Chemical Phenomena Collagen Type IV Humans Hydroxylysine Mass Spectrometry Methionine Models, Molecular Molecular Sequence Data Nitrogen Nuclear Magnetic Resonance, Biomolecular Protein Conformation Protein Multimerization Protein Subunits Sequence Alignment Stress, Mechanical Sulfur

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